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Quantification of matrix metalloproteinases and tissue inhibitors of metalloproteinase in prostatic tissue: Analytical aspects
Author(s) -
Jung Klaus,
Lein Michael,
Ulbrich Norbert,
Rudolph Birgit,
Henke Wolfgang,
Schnorr Dietmar,
Loening Stefan A.
Publication year - 1998
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/(sici)1097-0045(19980201)34:2<130::aid-pros8>3.0.co;2-o
Subject(s) - matrix metalloproteinase , prostate , matrix (chemical analysis) , extraction (chemistry) , chemistry , pathology , medicine , cancer , chromatography , biochemistry
BACKGROUND The balance between matrix metalloproteinases (MMP) and the tissue inhibitors of metalloproteinases (TIMP) has been seen as important during tumor invasion and progression. The determination of these components needs a special strategy of tissue preparation. This analytical problem has not been considered for prostatic tissue. METHODS We adapted an extraction method consisting of two extraction steps with 0.25% Triton X‐100/CaCl 2 solution and two heat extraction steps at 60°C for 4 min. This combination allowed a complete extraction of MMP (measured as enzyme activity) and TIMP‐1 (measured with an ELISA test) from cancerous and normal prostatic tissue samples. RESULTS The median values for cancerous vs. normal MMPs (50.8 mU/g wet tissue and 1,580 mU/g protein vs. 88.8 and 2,497) and TIMP‐1 (4.49 μg/g wet tissue and 96.7 μg/g protein vs. 12.4 and 237.8) were significantly lower, whereas the respective ratios for MMP/TIMP‐1 (11.1 vs. 4.0 on wet weight and 15.5 vs. 5.3 on protein basis) were significantly higher. CONCLUSIONS An optimized extraction procedure was elaborated for determining MMPs and TIMP‐1 in prostatic tissue samples. The increased ratio of MMP/TIMP‐1 can be interpreted as an indicator of the imbalance between MMP and TIMP, characteristic of prostate carcinoma tissue. Prostate 34:130–136, 1998. © 1998 Wiley‐Liss, Inc.